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Gene Review

DPP4  -  dipeptidyl-peptidase 4

Bos taurus

Synonyms: CD26, DPPIV
 
 
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Disease relevance of DPP4

 

High impact information on DPP4

  • By 18 months, however, subsets of gammadelta T cells from both control and infected animals showed an increase in expression of CD25, ACT2, and CD26 in the presence of the antigens [2].
  • CD4(+) T cells with a memory phenotype (CD45R0(+)) expressing CD25 and CD26 were the predominant cell type responding to antigens [2].
  • CD26 is expressed on a restricted subpopulation of dendritic cells in vivo [3].
  • A cDNA encoding bovine CD26 was cloned and the recombinant molecule expressed in COS-7 cells [3].
  • The peptidase cleaved the standard DPIV substrate, Gly-Pro-MCA with a K(M) of 38.4 microM, while Lys-Pro-MCA was hydrolysed with a K(M) of 103 microM [4].
 

Biological context of DPP4

  • Most CD8(+) T cells in cultures of bovine mononuclear cells stimulated with staphylococcal enterotoxin C1 develop an unusual phenotype characterized by expression of activation molecule 3 (ACT3) [5].
  • These results demonstrate that ACT3 is identical to BoCD26 and suggest that CD26 upregulation on CD8(+) T cells is a general phenomenon of superantigens and not limited to their effects on bovine cells [6].
 

Anatomical context of DPP4

 

Associations of DPP4 with chemical compounds

  • DPIV-like activity was not inhibited by serine protease inhibitors but was by the metallo-protease inhibitors, the phenanthrolines [4].
  • The DPIV-like activity was specifically inhibited by both Diprotin A and B, non-competitively, generating a K(i) of 1.4 x 10(-4) M for both inhibitors [4].
  • Repeated injections of more than 10 micrograms of Ala-boroPro or Pro-boroPro at 12 h intervals maintained in vivo DP IV activity at less than 30% of the normal level [10].
  • Especially, the release of proline increases drastically from almost zero to the theoretical amount in the presence of DP IV [11].
  • These milk T lymphocytes are mature CD4+, or CD8+ single positive T cells, expressing CD44, CD26, and beta 1 integrin, but not Lam-1 [12].
 

Physical interactions of DPP4

 

Other interactions of DPP4

 

Analytical, diagnostic and therapeutic context of DPP4

References

  1. Early induction of humoral and cellular immune responses during experimental Mycobacterium avium subsp. paratuberculosis infection of calves. Waters, W.R., Miller, J.M., Palmer, M.V., Stabel, J.R., Jones, D.E., Koistinen, K.A., Steadham, E.M., Hamilton, M.J., Davis, W.C., Bannantine, J.P. Infect. Immun. (2003) [Pubmed]
  2. Analysis of the immune response to Mycobacterium avium subsp. paratuberculosis in experimentally infected calves. Koo, H.C., Park, Y.H., Hamilton, M.J., Barrington, G.M., Davies, C.J., Kim, J.B., Dahl, J.L., Waters, W.R., Davis, W.C. Infect. Immun. (2004) [Pubmed]
  3. CD26 is expressed on a restricted subpopulation of dendritic cells in vivo. Gliddon, D.R., Howard, C.J. Eur. J. Immunol. (2002) [Pubmed]
  4. The purification and characterisation of novel dipeptidyl peptidase IV-like activity from bovine serum. Buckley, S.J., Collins, P.J., O'Connor, B.F. Int. J. Biochem. Cell Biol. (2004) [Pubmed]
  5. Identity of activation molecule 3 on superantigen-stimulated bovine cells is CD26. Lee, S.U., Ferens, W., Davis, W.C., Hamilton, M.J., Park, Y.H., Fox, L.K., Naessens, J., Bohach, G.A. Infect. Immun. (2001) [Pubmed]
  6. Molecular characterization of bovine CD26 upregulated by a staphylococcal superantigen. Lee, S.U., Park, Y.H., Davis, W.C., Hamilton, J., Naessens, J., Bohach, G.A. Immunogenetics (2002) [Pubmed]
  7. Adenosine deaminase in rodent median eminence: detection by antibody to the mouse enzyme and co-localization with adenosine deaminase-complexing protein (CD26). Nagy, J.I., Yamamoto, T., Uemura, H., Schrader, W.P. Neuroscience (1996) [Pubmed]
  8. Evidence for receptor-mediated uptake of adenosine deaminase in rabbit kidney. Schrader, W.P., Miczek, A.D., West, C.A., Samsonoff, W.A. J. Histochem. Cytochem. (1988) [Pubmed]
  9. Dipeptidyl peptidases in bovine reproductive organs and secretions. Agrawal, Y., Vanha-Perttula, T. Int. J. Androl. (1986) [Pubmed]
  10. Involvement of dipeptidyl peptidase IV in an in vivo immune response. Kubota, T., Flentke, G.R., Bachovchin, W.W., Stollar, B.D. Clin. Exp. Immunol. (1992) [Pubmed]
  11. Complementary action of dipeptidyl peptidase IV and aminopeptidase M in the digestion of beta-casein. Heymann, E., Mentlein, R. J. Dairy Res. (1986) [Pubmed]
  12. Characterisation of leucocytic somatic cells in bovine milk. Schmaltz, R., Bhogal, B., Wang, J., Wang, Y.Y., Mackay, C.R., Chen, S.S., Larson, L. Res. Vet. Sci. (1996) [Pubmed]
  13. On the regulatory role of dipeptidyl peptidase IV (=CD=adenosine deaminase complexing protein) on adenosine deaminase activity. Ben-Shooshan, I., Kessel, A., Ben-Tal, N., Cohen-Luria, R., Parola, A.H. Biochim. Biophys. Acta (2002) [Pubmed]
  14. Study of the enzymatic degradation of vasostatin I and II and their precursor chromogranin A by dipeptidyl peptidase IV using high-performance liquid chromatography/electrospray mass spectrometry. Zhang, X.Y., De Meester, I., Lambeir, A.M., Dillen, L., Van Dongen, W., Esmans, E.L., Haemers, A., Scharpé, S., Claeys, M. Journal of mass spectrometry : JMS. (1999) [Pubmed]
 
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